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The CLAVATA1 (CLV1) receptor kinase regulates stem cell specification at shoot

The CLAVATA1 (CLV1) receptor kinase regulates stem cell specification at shoot and flower meristems of Arabidopsis. the meristem flanks. THE vast majority of tissues and organs of the adult plant are formed postembryonically. To achieve continuous organ formation plants rely on the activity of stem cells located at meristems (Byrne 2003; Carles and Fletcher 2003; Gross-Hardt and Laux 2003). The shoot apical meristem, which produces the aerial portion of the plant, is composed of a central pool of stem cells surrounded by descendant cells that are directed toward differentiation. Division of stem cells results in daughter cells that maintain the central stem cell population as well as daughter cells that are localized more peripherally, where they perceive positional cues that drive their differentiation. Stem cell specification and organogenesis at the Arabidopsis shoot apical meristem is regulated by a receptor-kinase signaling system that includes the (gene products. encodes a receptor-kinase protein with 21 leucine-rich repeats (LRRs) in its predicted extracellular domain, a single pass transmembrane domain, and a cytoplasmic serine/threonine kinase domain (Clark 1997). encodes a proteins just like CLV1 structurally, however CLV2 includes a very small expected cytoplasmic site without known signaling motifs (Jeong 1999). CLV1 build up reaches least partly reliant on the current presence of CLV2 (Jeong 1999). Furthermore, CLV1 and CLV2 are hypothesized to create a heterodimer based on migration in both gel chromatography and non-reducing proteins gel blots (Trotochaud 1999). Many lines of proof claim that CLV3 may be the ligand SB 203580 price for CLV1. CLV3 can be both shows up and secreted to go through proteolytic maturation, liberating a conserved polypetide, termed the CLV3/ESR-related (CLE) site, through the C terminus that’s capable of changing vegetable advancement when added exogenously (Fiers 2005; Ito 2006; Kondo 2006; Ni and Clark 2006). Null mutations in are mainly epistatic to mutations in and overexpression phenotypes are reliant on CLV1, recommending that CLV3 features upstream of CLV1 (Clark 1995; Brand 2000). Furthermore, CLV3 is necessary for the forming of a big molecular mass complicated including CLV1 (Trotochaud 1999). CLV1 works to limit the diffusion of CLV3 proteins, recommending that CLV1 binds to CLV3, sequestering it (Lenhard and Laux 2003). Latest work shows how the CLE peptide can be with the capacity of binding towards the CLV1 extracellular site (Ogawa 2008). Used collectively these data recommend a model where CLV1 and CLV2 type a receptor complicated that’s with the capacity of activating particular sign transduction pathways upon notion from the CLE peptide produced from CLV3. function inside a common hereditary pathway to modify the expression site from the stem cell-promoting transcription element, (1998; Brand 2000; Schoof 2000). Mutations in bring about an increased manifestation site and a more substantial meristem with extra stem cells (Clark 1993, 1995; Clark and Kayes 1998; Brand 2000; Schoof 2000), while mutations in bring about reduction SB 203580 price or eradication of the meristem (Laux 1996). The related phosphatases POLTERGEIST (POL) and PLL1 are signaling intermediates acting downstream of CLV1, CLV2, and CLV3. POL/PLL1 act to maintain expression within the meristem, while CLV signaling represses POL/PLL1 activity (Yu 2000, 2003; SB 203580 price Song and Clark 2005; Song 2006). The remaining genetic and biochemical mechanisms that link CLV1 activation and expression are largely unknown. Several lines of evidence suggest the presence of additional receptors that function in parallel with CLV1. Most of the mutant alleles identified in mutagenic screens are dominant-negative missense alleles Mouse monoclonal to LPP that exhibit intermediate-to-strong phenotypes, while null alleles exhibit quite weak phenotypes by comparison (Divart 2003). In addition, null alleles exhibit strong meristem phenotypes.